Dataset Information
Type six secretion system exported effector 5 (Tse5)
Ontology highlight
ABSTRACT:
SUBMITTER: David Albesa-Jove
PROVIDER: EMPIAR-12296 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.
Nature communications 20231128 1
Bacterial competition is a significant driver of toxin polymorphism, which allows continual compensatory evolution between toxins and the resistance developed to overcome their activity. Bacterial Rearrangement hot spot (Rhs) proteins represent a widespread example of toxin polymorphism. Here, we present the 2.45 Å cryo-electron microscopy structure of Tse5, an Rhs protein central to Pseudomonas aeruginosa type VI secretion system-mediated bacterial competition. This structural insight, coupled ...[more]